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Database: UniProt
Entry: D3PTL8_MEIRD
LinkDB: D3PTL8_MEIRD
Original site: D3PTL8_MEIRD 
ID   D3PTL8_MEIRD            Unreviewed;       266 AA.
AC   D3PTL8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AGK05750.1};
DE            EC=2.7.4.7 {ECO:0000313|EMBL:ADD28801.1};
GN   OrderedLocusNames=Mrub_2046 {ECO:0000313|EMBL:ADD28801.1};
GN   ORFNames=K649_12310 {ECO:0000313|EMBL:AGK05750.1};
OS   Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS   ruber).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK05750.1, ECO:0000313|Proteomes:UP000013026};
RN   [1] {ECO:0000313|EMBL:ADD28801.1, ECO:0000313|Proteomes:UP000006655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC   {ECO:0000313|EMBL:ADD28801.1};
RX   PubMed=21304689; DOI=10.4056/sigs.1032748;
RA   Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Meiothermus ruber type strain (21).";
RL   Stand. Genomic Sci. 3:26-36(2010).
RN   [2] {ECO:0000313|EMBL:AGK05750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK05750.1};
RA   Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA   Eichler E., Turner S.W.;
RT   "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT   Sequencing Data.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGK05750.1, ECO:0000313|Proteomes:UP000013026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC   {ECO:0000313|EMBL:AGK05750.1};
RA   Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC         amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC         Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC         methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC         Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC         EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; CP001743; ADD28801.1; -; Genomic_DNA.
DR   EMBL; CP005385; AGK05750.1; -; Genomic_DNA.
DR   RefSeq; WP_013014299.1; NC_021081.1.
DR   AlphaFoldDB; D3PTL8; -.
DR   STRING; 504728.K649_12310; -.
DR   KEGG; mrb:Mrub_2046; -.
DR   KEGG; mre:K649_12310; -.
DR   PATRIC; fig|504728.9.peg.2534; -.
DR   eggNOG; COG0351; Bacteria.
DR   OrthoDB; 9810880at2; -.
DR   Proteomes; UP000006655; Chromosome.
DR   Proteomes; UP000013026; Chromosome.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AGK05750.1};
KW   Transferase {ECO:0000313|EMBL:ADD28801.1}.
FT   DOMAIN          13..256
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   266 AA;  27543 MW;  3185A952B137C6FF CRC64;
     MPFPIALTIA GSDPSGGAGL QADLKTFHRF GVYGMSVVTV LTVQNTLGVR EVAPLEPGLV
     ARQLEAVLQD PGAHAIKTGA LGDAAIVHSI APILAQTNLP LVVDPVLVAK SGDWLLTEQA
     LEALKSELFP LATLLTPNLP EARALLGQPI RDLADAREAA RLLGGLGPRA VLLKGGHLAG
     EESTDVLWDG RKLHLFTAQK IPSSHTHGTG CTLSAAITAL LAKGVALLEA VARAKRFVTR
     AIETAPGIGG GIGPLNHWAE EGAENP
//
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